ID   A0A0M8N6L3_9HYPO        Unreviewed;       573 AA.
AC   A0A0M8N6L3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=ESCO_004110 {ECO:0000313|EMBL:KOS21050.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21050.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS21050.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|RuleBase:RU000672};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC       ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOS21050.1}.
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DR   EMBL; LGSR01000013; KOS21050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N6L3; -.
DR   STRING; 150374.A0A0M8N6L3; -.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000053831; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          178..573
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        336
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         336
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   573 AA;  64368 MW;  813F52FABC92D5E4 CRC64;
     MVPFLEAEHA GELDTLSERP PRLALAQYSV INPGLYCHFT TVVHINAQAI RNSNAFQEAM
     SEFALPEGFQ LAMDSWPFGG RSEDDVDDGR YWGGLVFAKP VTPVDSNYYA YPIPITVMVD
     ARTMEVIRVE RFATGGVGDG LRPSPRRDTP RKLFEDHRGA EYLPENICIP LRSDLKPIHI
     TQPKGASFRV HSDRLIEWQK WSFRLGFNAR EGAVLHDVCY DGRPIFYRLS FSEMTVPYAD
     PRPPFQRKQA FDFGDVGVGR TANNLQLGCD CLGAIHYVDA IDVNSDGSPQ TSKTVVCIHE
     QDNGILWKHT DVRTNRSGIV RNREFIVQFI ATLGNYEYIL SYTLDLAGGI SMETRATGIV
     SVAAIDLGKT SEYGNVVSPG ILAQNHQHIF AARIDAAIDS YETGDTRVVV EDSVGRKICP
     DTNPYGNLYE VERKPVDEPT WIDLEPRLNR LIKLENTRKK NHVSGRHLAY KVVAPVTQLL
     LADDDSMAAK RARFAQHHLW VTGHRDGELY AAGDYTNMSS RETGGVSDMI KRPDRFAVDE
     LQLDEDDGHR AHPIVWVVFG LTHNPRVEDW PVM
//